ID A0A1I5MB40_9RHOB Unreviewed; 398 AA.
AC A0A1I5MB40;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alanine-glyoxylate transaminase / serine-glyoxylate transaminase / serine-pyruvate transaminase {ECO:0000313|EMBL:SFP06804.1};
GN ORFNames=SAMN04488047_102188 {ECO:0000313|EMBL:SFP06804.1};
OS Tranquillimonas alkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=441119 {ECO:0000313|EMBL:SFP06804.1, ECO:0000313|Proteomes:UP000199356};
RN [1] {ECO:0000313|EMBL:SFP06804.1, ECO:0000313|Proteomes:UP000199356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19547 {ECO:0000313|EMBL:SFP06804.1,
RC ECO:0000313|Proteomes:UP000199356};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; FOXA01000002; SFP06804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5MB40; -.
DR STRING; 441119.SAMN04488047_102188; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000199356; Unassembled WGS sequence.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:SFP06804.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199356}.
FT DOMAIN 64..325
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 398 AA; 42813 MW; A04503BC4B29749E CRC64;
MSLAAGREYL AIPGPSVVPD RVLRAMHRAS PNIYEGSLLE MAPTIQADLK RVARTEGDCA
IYIANGHGAW EAALSNTMSR GDAVLVLATG RFALGWSEVA RRLGLEVEVI DFGKRADADL
DRVAEALKGD AAHRFKAVLT VQTDTASSVR NDIPGLRRVL DDAGHPALLM VDCIACLACD
RFEMDAWGVD VTVAASQKGL MTPPGLSFVW FNKKAAQARE TADLATFYWD WQPRAEPAEF
YQFFGGTAPT HHLFGLRESL DMIFEEGLEN VWDRHATLAR AVWAAFEAWG ADGPLELNIA
DPAKRSHAVT AVRVGGPQGT EIRRWVMDNA GLTLGIGLGM AEKSSPEWHN FFRIAHMGHV
NAHMVLGALG SIQASLKAVG VPHGPGALDA AAEVCAGG
//